NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|45549285|ref|NP_525106|]
View 

DNA polymerase interacting tpr containing protein of 47kD, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CTWD_Cns1 cd21380
C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1 and ...
 232-387 6.07e-53

C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1 and similar proteins; Cns1, also called cyclophilin seven suppressor 1, or STI1 stress-inducible protein homolog, binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). It stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. It is involved in only a subset of Hsp90 functions. The model corresponds to Cns1 C-terminal wheel domain consisting of a twisted five-stranded beta sheet surrounded by several alpha helices.


:

Pssm-ID: 439174  Cd Length: 153  Bit Score: 173.13  E-value: 6.07e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 232 HRLRDAIEQRAIKFDDQKVGKKDVLSeeLLYPKFLPLEDHPVHLDEDGsTLIWPAAFSYPEFLYSDFYQQLPETTTMRDC 311
Cdd:cd21380   1 EKLIKAIKERGIKLEGSKKGESDDLS--LLEPCHPELSGARVHLDEEG-RLVWPVLFLYPEYKQSDFIQAFHEDTTFIDH 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45549285 312 LATLLTEKLPYDKAHNYRLGNVHVYYENRKVGCVHKVDEEKQLAEIIAEKGFFVSGGALLFYVVHKDSRVEQEFIN 387
Cdd:cd21380  78 LEVMFEEPPPWDVEKKYTPDNLNVYFEDRDKGKLVKVDPKSTLGEVLSHKRYVVKNGTPSFIVLVKGSEFEKEFLK 153
3a0801s09 super family cl36792
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 84-179 3.25e-08

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


The actual alignment was detected with superfamily member TIGR00990:

Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 55.38  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285    84 ENTRDELALNYKEDGNFYMKHKKFRMAIYSFTEGIKTKTDnpdvlAVLYNNRSAAHFFIKNYRSSLSDAQRALFYKPDYT 163
Cdd:TIGR00990 120 EEERKKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPD-----PVYYSNRAACHNALGDWEKVVEDTTAALELDPDYS 194

                          90
                  ....*....|....*.
gi 45549285   164 KARWRSAQCAYELERF 179
Cdd:TIGR00990 195 KALNRRANAYDGLGKY 210
 
Name Accession Description Interval E-value
CTWD_Cns1 cd21380
C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1 and ...
 232-387 6.07e-53

C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1 and similar proteins; Cns1, also called cyclophilin seven suppressor 1, or STI1 stress-inducible protein homolog, binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). It stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. It is involved in only a subset of Hsp90 functions. The model corresponds to Cns1 C-terminal wheel domain consisting of a twisted five-stranded beta sheet surrounded by several alpha helices.


Pssm-ID: 439174  Cd Length: 153  Bit Score: 173.13  E-value: 6.07e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 232 HRLRDAIEQRAIKFDDQKVGKKDVLSeeLLYPKFLPLEDHPVHLDEDGsTLIWPAAFSYPEFLYSDFYQQLPETTTMRDC 311
Cdd:cd21380   1 EKLIKAIKERGIKLEGSKKGESDDLS--LLEPCHPELSGARVHLDEEG-RLVWPVLFLYPEYKQSDFIQAFHEDTTFIDH 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45549285 312 LATLLTEKLPYDKAHNYRLGNVHVYYENRKVGCVHKVDEEKQLAEIIAEKGFFVSGGALLFYVVHKDSRVEQEFIN 387
Cdd:cd21380  78 LEVMFEEPPPWDVEKKYTPDNLNVYFEDRDKGKLVKVDPKSTLGEVLSHKRYVVKNGTPSFIVLVKGSEFEKEFLK 153
Wheel pfam18972
Cns1/TTC4 Wheel domain; The wheel domain is found at the C-terminus of yeast Cns1 and human ...
 280-388 5.38e-16

Cns1/TTC4 Wheel domain; The wheel domain is found at the C-terminus of yeast Cns1 and human TTC4 proteins. The structure of the domain shows an overall fold consisting of a twisted five-stranded beta sheet surrounded by several alpha helices. The Hsp90 chaperone machinery in eukaryotes comprises a number of distinct accessory factors. Cns1 is one of the few essential co-chaperones in yeast. Cns1 is important for maintaining translation elongation, specifically chaperoning the elongation factor eEF2. In this context, Cns1 interacts with the novel co-factor Hgh1 and forms a quaternary complex together with eEF2 and Hsp90.


Pssm-ID: 436877  Cd Length: 114  Bit Score: 73.41  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285   280 STLIWPAAFSYPEFLYSDFYQQLPETTTMRDCLATLLTEKLPYDKAHNYRLGNVHVYYENRKVGCVhKVDEEKQLAEIIA 359
Cdd:pfam18972   7 STLIFPVFFLYPLHAQSDFIKAFSETTTPQDHLEYVFPSPPPWDTKKEYTPKNVEVYMETRTGGLV-KVGKKVPLRKVLS 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 45549285   360 -EKGFFVSGGALLFYVVHKDSRveQEFINE 388
Cdd:pfam18972  86 sAPKVELVDGLLRIYVVPKGKA--QKWIED 113
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 84-179 3.25e-08

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 55.38  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285    84 ENTRDELALNYKEDGNFYMKHKKFRMAIYSFTEGIKTKTDnpdvlAVLYNNRSAAHFFIKNYRSSLSDAQRALFYKPDYT 163
Cdd:TIGR00990 120 EEERKKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPD-----PVYYSNRAACHNALGDWEKVVEDTTAALELDPDYS 194

                          90
                  ....*....|....*.
gi 45549285   164 KARWRSAQCAYELERF 179
Cdd:TIGR00990 195 KALNRRANAYDGLGKY 210
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
78-227 1.93e-07

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 51.45  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285  78 LKYDPEENTRDELALNYKEDGNFYMKHKKFRMAIYSFTEGIKTKTDNPDVlavlYNNRSAAHFFIKNYRSSLSDAQRALF 157
Cdd:COG4785  60 AERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEA----YNNRGLAYLLLGDYDAALEDFDRALE 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 158 YKPDYTKARWRSAQCAYELERFDL----------------CTQMCEELLEVDVDNEVAIALLHKNKMKKLEIErNQRKEA 221
Cdd:COG4785 136 LDPDYAYAYLNRGIALYYLGRYELaiadlekaleldpndpERALWLYLAERKLDPEKALALLLEDWATAYLLQ-GDTEEA 214


                ....*.
gi 45549285 222 AEAKRR 227
Cdd:COG4785 215 RELFKL 220
 
Name Accession Description Interval E-value
CTWD_Cns1 cd21380
C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1 and ...
 232-387 6.07e-53

C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1 and similar proteins; Cns1, also called cyclophilin seven suppressor 1, or STI1 stress-inducible protein homolog, binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). It stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. It is involved in only a subset of Hsp90 functions. The model corresponds to Cns1 C-terminal wheel domain consisting of a twisted five-stranded beta sheet surrounded by several alpha helices.


Pssm-ID: 439174  Cd Length: 153  Bit Score: 173.13  E-value: 6.07e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 232 HRLRDAIEQRAIKFDDQKVGKKDVLSeeLLYPKFLPLEDHPVHLDEDGsTLIWPAAFSYPEFLYSDFYQQLPETTTMRDC 311
Cdd:cd21380   1 EKLIKAIKERGIKLEGSKKGESDDLS--LLEPCHPELSGARVHLDEEG-RLVWPVLFLYPEYKQSDFIQAFHEDTTFIDH 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45549285 312 LATLLTEKLPYDKAHNYRLGNVHVYYENRKVGCVHKVDEEKQLAEIIAEKGFFVSGGALLFYVVHKDSRVEQEFIN 387
Cdd:cd21380  78 LEVMFEEPPPWDVEKKYTPDNLNVYFEDRDKGKLVKVDPKSTLGEVLSHKRYVVKNGTPSFIVLVKGSEFEKEFLK 153
CTWD_Cns1-like cd21377
C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1, Homo ...
 233-386 4.77e-23

C-terminal wheel domain found in Saccharomyces cerevisiae Hsp70/Hsp90 co-chaperone Cns1, Homo sapiens tetratricopeptide repeat protein 4 (TTC4), and similar proteins; The family includes Hsp70/Hsp90 co-chaperone Cns1 from Saccharomyces cerevisiae and the human Cns1 homolog tetratricopeptide repeat protein 4 (TTC4), both of which contain a C-terminal wheel domain consisting of a twisted five-stranded beta sheet surrounded by several alpha helices. Cns1, also called cyclophilin seven suppressor 1, or STI1 stress-inducible protein homolog, binds to the molecular chaperones Hsp90 (HSC82 and HSP82) and Hsp70 (SSA1). It stimulates SSA1 ATPase activity, but not Hsp90 ATPase activity. It is involved in only a subset of Hsp90 functions. TTC4, also called TPR repeat protein 4, is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells. It interacts with TBK1 and promotes Sendai virus (SeV)-induced host cell innate immune responses.


Pssm-ID: 439173  Cd Length: 159  Bit Score: 94.33  E-value: 4.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 233 RLRDAIEQRAIKfddqkVGKKdvlseelLYPKFLPlEDHPVHLDEDGStLIWPAAFSYPEFLYSDFYQQLPETTTMRDCL 312
Cdd:cd21377   2 ALLSALKSRGIK-----LGPP-------LYDEELT-GERKPYLDEDGE-LHWPVLLLYPEVGQSDFIEDFSEDDTLGDHL 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 313 ATLLTEK---LPYDKAHNYRLGNVHVYYE---------------NRKVGCVhKVDEEKQLAEIIAEKGFFVSGGALLFYV 374
Cdd:cd21377  68 DVMFPEPappLPWDTEGEYTRDNLEVYYEtnavkplpsesskagPKEKKWV-RVDPDTTLGDVLAHPDYYVIPGIPVFYV 146

                       170
                ....*....|..
gi 45549285 375 VHKDSRVEQEFI 386
Cdd:cd21377 147 VPKGSPFEKRFL 158
Wheel pfam18972
Cns1/TTC4 Wheel domain; The wheel domain is found at the C-terminus of yeast Cns1 and human ...
 280-388 5.38e-16

Cns1/TTC4 Wheel domain; The wheel domain is found at the C-terminus of yeast Cns1 and human TTC4 proteins. The structure of the domain shows an overall fold consisting of a twisted five-stranded beta sheet surrounded by several alpha helices. The Hsp90 chaperone machinery in eukaryotes comprises a number of distinct accessory factors. Cns1 is one of the few essential co-chaperones in yeast. Cns1 is important for maintaining translation elongation, specifically chaperoning the elongation factor eEF2. In this context, Cns1 interacts with the novel co-factor Hgh1 and forms a quaternary complex together with eEF2 and Hsp90.


Pssm-ID: 436877  Cd Length: 114  Bit Score: 73.41  E-value: 5.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285   280 STLIWPAAFSYPEFLYSDFYQQLPETTTMRDCLATLLTEKLPYDKAHNYRLGNVHVYYENRKVGCVhKVDEEKQLAEIIA 359
Cdd:pfam18972   7 STLIFPVFFLYPLHAQSDFIKAFSETTTPQDHLEYVFPSPPPWDTKKEYTPKNVEVYMETRTGGLV-KVGKKVPLRKVLS 85

                          90       100       110
                  ....*....|....*....|....*....|
gi 45549285   360 -EKGFFVSGGALLFYVVHKDSRveQEFINE 388
Cdd:pfam18972  86 sAPKVELVDGLLRIYVVPKGKA--QKWIED 113
CTWD_TTC4 cd21381
C-terminal wheel domain found in Homo sapiens tetratricopeptide repeat protein 4 (TTC4) and ...
 268-388 5.50e-12

C-terminal wheel domain found in Homo sapiens tetratricopeptide repeat protein 4 (TTC4) and similar proteins; TTC4, also called TPR repeat protein 4, is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells. It interacts with TBK1 and promotes Sendai virus (SeV)-induced host cell innate immune responses. The model corresponds to TTC4 C-terminal wheel domain consisting of a twisted five-stranded beta sheet surrounded by several alpha helices.


Pssm-ID: 439175  Cd Length: 150  Bit Score: 63.30  E-value: 5.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 268 LEDHPVHLDED---GSTLIWPAAFSYPEFLYSDFYQQLPETTTMRDCLATLLTEKLPYDKAHNYRLGNVHVYYENRKVGC 344
Cdd:cd21381  29 LEDAKILLEDPldpESQLIFPALLLYPLHLQSDFIKAFSELSTPQEHLEYVLPRPWDWDKHEEYTPKNVECYMETESGGL 108

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 45549285 345 VhKVDEEKQLAEIIAEKGFFVSGGALLFYVVHKDSRveQEFINE 388
Cdd:cd21381 109 V-KVGKKVPLLKVLSNGKVPLFDGLLRIYVVPKNKA--AEWIKE 149
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 84-179 3.25e-08

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 55.38  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285    84 ENTRDELALNYKEDGNFYMKHKKFRMAIYSFTEGIKTKTDnpdvlAVLYNNRSAAHFFIKNYRSSLSDAQRALFYKPDYT 163
Cdd:TIGR00990 120 EEERKKYAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKPD-----PVYYSNRAACHNALGDWEKVVEDTTAALELDPDYS 194

                          90
                  ....*....|....*.
gi 45549285   164 KARWRSAQCAYELERF 179
Cdd:TIGR00990 195 KALNRRANAYDGLGKY 210
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
78-227 1.93e-07

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 51.45  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285  78 LKYDPEENTRDELALNYKEDGNFYMKHKKFRMAIYSFTEGIKTKTDNPDVlavlYNNRSAAHFFIKNYRSSLSDAQRALF 157
Cdd:COG4785  60 AERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEA----YNNRGLAYLLLGDYDAALEDFDRALE 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 158 YKPDYTKARWRSAQCAYELERFDL----------------CTQMCEELLEVDVDNEVAIALLHKNKMKKLEIErNQRKEA 221
Cdd:COG4785 136 LDPDYAYAYLNRGIALYYLGRYELaiadlekaleldpndpERALWLYLAERKLDPEKALALLLEDWATAYLLQ-GDTEEA 214


                ....*.
gi 45549285 222 AEAKRR 227
Cdd:COG4785 215 RELFKL 220
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
83-262 2.18e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.46  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285  83 EENTRDELALNYKedGNFYMKHKKFRMAIYSFTEGIKTKTDNPDVlavlYNNRSAAHFFIKNYRSSLSDAQRALFYKPDY 162
Cdd:COG0457  70 ELDPDDAEALNNL--GLALQALGRYEEALEDYDKALELDPDDAEA----LYNLGLALLELGRYDEAIEAYERALELDPDD 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285 163 TKARWRSAQCAYELERFDLCTQMCEELLEVDVDNEVAIALLHKNKMKKLEIERNQRKEAAEAKRRLTRFHRLRDAIEQRA 242
Cdd:COG0457 144 ADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELL 223

                       170       180
                ....*....|....*....|
gi 45549285 243 IKFDDQKVGKKDVLSEELLY 262
Cdd:COG0457 224 LLALALLLALRLAALALYQY 243
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 76-202 8.15e-05

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 41.92  E-value: 8.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285  76 QKLKYDPEeNTRDELALnykedGNFYMKHKKFRMAIYSFTEGIKTKTDNPDVLAvlynNRSAAHFFIKNYRSSLSDAQRA 155
Cdd:COG4235   8 QALAANPN-DAEGWLLL-----GRAYLRLGRYDEALAAYEKALRLDPDNADALL----DLAEALLAAGDTEEAEELLERA 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 45549285 156 LFYKPDYTKARWRSAQCAYELERFDLCTQMCEELLEVDVDNEVAIAL 202
Cdd:COG4235  78 LALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADAPARLL 124
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 75-203 3.64e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.59  E-value: 3.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45549285  75 LQKLKYDPEENTRDELALNYKEDGNFYMKHKKFRMAIYSFTEGIKTKTDNPDVlavlYNNRSAAHFFIKNYRSSLSDAQR 154
Cdd:COG3914  62 LAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEA----LFNLGNLLLALGRLEEALAALRR 137

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 45549285 155 ALFYKPDYTKARWRSAQCAYELERFDLCTQMCEELLEVDVDNEVAIALL 203
Cdd:COG3914 138 ALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNL 186
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH